Linked Life Data

19320526

Source:http://linkedlifedata.com/resource/pubmed/id/19320526

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
2009-3-26
pubmed:abstractText
QM/MM models of the peroxo forms of vanadium-containing haloperoxidases (VHPOs) are critically assessed in terms of active site geometries, hydrogen bonds within the active site, isotropic and anisotropic (51)V NMR chemical shifts, and TD-DFT excitation energies. The geometric stability within the active site of the protein is comparable to the respective native forms, as indicated by low standard deviations in bond lengths across a number of local minima sampled along MD trajectories. There is a significant calculated upfield shift in delta((51)V) upon formation of the peroxo from the respective native forms for both the vanadium-containing chloroperoxidase (VCPO) and vanadium-containing bromoperoxidase (VBPO) models, which is in qualitative agreement with (51)V NMR experiments of VBPO in solution. The models show appreciable differences between the anisotropic chemical shifts of the different protonation states of the peroxo form of VHPO. The most likely candidates for the peroxo forms of the VHPO enzymes appear to be unprotonated or have a single proton on either of the equatorial oxygen ligands, based on QM/MM modeling in combination with X-ray, (51)V NMR, and UV-vis data.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1520-6106
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
113
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4456-65
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
51V NMR chemical shifts calculated from QM/MM models of peroxo forms of vanadium haloperoxidases.
pubmed:affiliation
Max-Planck-Institut fur Kohlenforschung, Kaiser-Wilhelm-Platz, Mulheim an der Ruhr, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't